DOI: 10.1042/bj2250707. Molecular cloning of a bovine cathepsin

10.1042/bj2250707

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

Abstract

A cDNA clone for a thiol endoproteinase has been isolated from a bovine heart cDNA library by using a mixture of 32 synthetic oligonucleotides as a hybridization probe. The inserted region is 672 base pairs in length. It contains a sequence encoding the C-terminal region of a protein that is homologous to rat liver cathepsins B and H and to plant thiol proteinases. In addition, it contains the sequence of 442 bases corresponding to the 3′ untranslated region of the mRNA. The inserted region was used as a specific probe in RNA transfer analysis; the size of the mRNA encoding the thiol endoproteinase is estimated to be approx. 1.7 kilobases. Thus, the maximum size of the encoded protein is about 350-400 amino acids.

Bibliography

Gay, N. J., & Walker, J. E. (1985). Molecular cloning of a bovine cathepsin. Biochemical Journal, 225(3), 707â712.

Authors 2

N J Gay (first)
J E Walker (additional)

References 0 Referenced 17

None

Dates

Type	When
Created	10 years ago (Aug. 10, 2015, 4:48 p.m.)
Deposited	3 years, 9 months ago (Nov. 25, 2021, 9:52 a.m.)
Indexed	1 year, 10 months ago (Oct. 7, 2023, 5:20 a.m.)
Issued	40 years, 7 months ago (Feb. 1, 1985)
Published	40 years, 7 months ago (Feb. 1, 1985)
Published Print	40 years, 7 months ago (Feb. 1, 1985)

Funders 0

None

BibTeX

@article{Gay_1985, title={Molecular cloning of a bovine cathepsin}, volume={225}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2250707}, DOI={10.1042/bj2250707}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Gay, N J and Walker, J E}, year={1985}, month=feb, pages={707–712} }

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